Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
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International Union of Crystallography (IUCr)
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Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic proteins which, although lacking catalytic activity, possess the ability to disrupt biological membranes, inducing significant muscle-tissue loss and permanent disability in severely envenomed patients. Since the structural basis for their toxic activity is still only partially understood, the structure of myotoxin II, a monomeric Lys49 PLA2 homologue from Atropoides nummifer, has been determined at 2.08 Å resolution and the anion-binding site has been characterized. © 2006 International Union of Crystallography. All rights reserved.
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Atropoides nummifer , myotoxin II, Atropoides nummifer , phospholipase A , snake venom , amino acid sequence , binding site , chemistry , crystallization , molecular genetics , sequence alignment , X ray crystallography , Amino Acid Sequence , Binding Sites , Crotalid Venoms , Crystallization , Crystallography, X-Ray , Molecular Sequence Data , Phospholipases A , Sequence Alignment
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Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v. 62, n. 5, p. 423-426, 2006.
